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3mi3

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{{Seed}}
 
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[[Image:3mi3.jpg|left|200px]]
 
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==Homocitrate Synthase Lys4 bound to Lysine==
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The line below this paragraph, containing "STRUCTURE_3mi3", creates the "Structure Box" on the page.
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<StructureSection load='3mi3' size='340' side='right'caption='[[3mi3]], [[Resolution|resolution]] 2.38&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[3mi3]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Schizosaccharomyces_pombe Schizosaccharomyces pombe]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3l90 3l90]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MI3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3MI3 FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.38&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=LYS:LYSINE'>LYS</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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{{STRUCTURE_3mi3| PDB=3mi3 | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3mi3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mi3 OCA], [https://pdbe.org/3mi3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3mi3 RCSB], [https://www.ebi.ac.uk/pdbsum/3mi3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3mi3 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/HOSM_SCHPO HOSM_SCHPO]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/mi/3mi3_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3mi3 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The alpha-aminoadipate pathway of lysine biosynthesis is modulated at the transcriptional and biochemical levels by feedback inhibition. The first enzyme in the alpha-aminoadipate pathway, homocitrate synthase (HCS), is the target of the feedback regulation and is strongly inhibited by l-lysine. Here we report the structure of Schizosaccharomyces pombe HCS (SpHCS) in complex with l-lysine. The structure illustrates that the amino acid directly competes with the substrate 2-oxoglutarate for binding within the active site of HCS. Differential recognition of the substrate and inhibitor is achieved via a switch position within the (alpha/beta)(8) TIM barrel of the enzyme that can distinguish between the C5-carboxylate group of 2-oxoglutarate and the epsilon-ammonium group of l-lysine. In vitro and in vivo assays demonstrate that mutations of the switch residues, which interact with the l-lysine epsilon-ammonium group, abrogate feedback inhibition, as do substitutions of residues within the C-terminal domain that were identified in a previous study of l-lysine-insensitive HCS mutants in Saccharomyces cerevisiae. Together, these results yield new insights into the mechanism of feedback regulation of an enzyme central to lysine biosynthesis.
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===Homocitrate Synthase Lys4 bound to Lysine===
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Structural basis for L-lysine feedback inhibition of homocitrate synthase.,Bulfer SL, Scott EM, Pillus L, Trievel RC J Biol Chem. 2010 Apr 2;285(14):10446-53. Epub 2010 Jan 19. PMID:20089861<ref>PMID:20089861</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3mi3" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_20089861}}, adds the Publication Abstract to the page
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*[[Homocitrate synthase|Homocitrate synthase]]
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(as it appears on PubMed at http://www.pubmed.gov), where 20089861 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_20089861}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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3MI3 is a 2 chains structure with sequences from [http://en.wikipedia.org/wiki/Schizosaccharomyces_pombe Schizosaccharomyces pombe]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3l90 3l90]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MI3 OCA].
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==Reference==
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<ref group="xtra">PMID:20089861</ref><references group="xtra"/>
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[[Category: Homocitrate synthase]]
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[[Category: Schizosaccharomyces pombe]]
[[Category: Schizosaccharomyces pombe]]
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[[Category: Bulfer, S L.]]
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[[Category: Bulfer SL]]
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[[Category: Pillus, L.]]
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[[Category: Pillus L]]
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[[Category: Scott, E M.]]
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[[Category: Scott EM]]
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[[Category: Trievel, R C.]]
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[[Category: Trievel RC]]
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[[Category: Amino-acid biosynthesis]]
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[[Category: Claisen condensation]]
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[[Category: Lysine biosynthesis]]
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[[Category: Metalloprotein]]
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[[Category: Tim barrel]]
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[[Category: Transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Apr 28 10:42:40 2010''
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Current revision

Homocitrate Synthase Lys4 bound to Lysine

PDB ID 3mi3

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